ID   Y2476_GEOTN             Reviewed;         215 AA.
AC   A4IR67;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Uncharacterized methyltransferase GTNG_2476 {ECO:0000255|HAMAP-Rule:MF_02100};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN   OrderedLocusNames=GTNG_2476;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC   -!- FUNCTION: Could be a S-adenosyl-L-methionine-dependent
CC       methyltransferase. {ECO:0000255|HAMAP-Rule:MF_02100}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. YrrT family.
CC       {ECO:0000255|HAMAP-Rule:MF_02100}.
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DR   EMBL; CP000557; ABO67821.1; -; Genomic_DNA.
DR   RefSeq; WP_011887865.1; NC_009328.1.
DR   AlphaFoldDB; A4IR67; -.
DR   SMR; A4IR67; -.
DR   STRING; 420246.GTNG_2476; -.
DR   EnsemblBacteria; ABO67821; ABO67821; GTNG_2476.
DR   KEGG; gtn:GTNG_2476; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_111961_0_0_9; -.
DR   OMA; FEDWAAT; -.
DR   OrthoDB; 1739932at2; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_02100; Methyltr_YrrT; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023553; Uncharacterised_MeTfrase_YrrT.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..215
FT                   /note="Uncharacterized methyltransferase GTNG_2476"
FT                   /id="PRO_0000373854"
FT   BINDING         53
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
FT   BINDING         97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
SQ   SEQUENCE   215 AA;  24168 MW;  25D99A4AC0A89D84 CRC64;
     MGREFLDLFE QWAESYDQSV EGYDEQYRDV FAGYDRILST VADKAGQVVL EFGIGTGNLT
     KKLLERGKTV YGIEPSAPMR KKAAEKLGER AVIMDGDFLQ FPLPPEPIDT IASTYAFHHL
     TDAEKDEAIA KYSQLLHSGG KIVFADTAFR DKEAFRQTVE AARARGFHDL ADDLEREYYT
     TLDVLASLFA NHGFSVSFAQ QNAFVWVMEA VKQTT